PDBsum entry 1v6h

Structural genomics, unknown function

PDB id: 1v6h

Contents

Protein chains

103 a.a. *

Ligands

SO4

Waters ×386

* Residue conservation analysis

PDB id:

1v6h

Name:

Structural genomics, unknown function

Title:

The trimeric structure of divalent cation tolerance protein cuta1 from thermus thermophilus hb8

Structure:

Divalent cation tolerance protein cuta1. Chain: a, b, c. Engineered: yes

Source:

Thermus thermophilus. Organism_taxid: 274. Gene: cuta. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Biol. unit:

Trimer (from PQS)

Resolution:

1.90Å R-factor: 0.188 R-free: 0.234

Authors:

B.Bagautdinov,T.H.Tahirov,Riken Structural Genomics/proteomics Initiative (Rsgi)

Key ref:

B.Bagautdinov (2014). The structures of the CutA1 proteins from Thermus thermophilus and Pyrococcus horikoshii: characterization of metal-binding sites and metal-induced assembly. Acta Crystallogr F Struct Biol Commun, 70, 404-413. PubMed id: 24699729 DOI: 10.1107/S2053230X14003422

Date:

29-Nov-03 Release date: 23-Dec-03

Protein chains

Q7SIA8  (CUTA_THET8) -  Divalent-cation tolerance protein CutA from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)

Seq: 103 a.a.

Struc: 103 a.a.

DOI no: 10.1107/S2053230X14003422

Acta Crystallogr F Struct Biol Commun 70:404-413 (2014)

PubMed id: 24699729

The structures of the CutA1 proteins from Thermus thermophilus and Pyrococcus horikoshii: characterization of metal-binding sites and metal-induced assembly.

B.Bagautdinov.

ABSTRACT

CutA1 (copper tolerance A1) is a widespread cytoplasmic protein found in archaea, bacteria, plants and animals, including humans. In Escherichia coli it is implicated in divalent metal tolerance, while the mammalian CutA1 homologue has been proposed to mediate brain enzyme acetylcholinesterase activity and copper homeostasis. The X-ray structures of CutA1 from the thermophilic bacterium Thermus thermophilus (TtCutA1) with and without bound Na(+) at 1.7 and 1.9 Å resolution, respectively, and from the hyperthermophilic archaeon Pyrococcus horikoshii (PhCutA1) in complex with Na(+) at 1.8 Å resolution have been determined. Both are short and rigid proteins of about 12 kDa that form intertwined compact trimers in the crystal and solution. The main difference in the structures is a wide-type β-bulge on top of the TtCutA1 trimer. It affords a mechanism for lodging a single-residue insertion in the middle of β2 while preserving the interprotomer main-chain hydrogen-bonding network. The liganded forms of the proteins provide new structural information about the metal-binding sites and CutA1 assembly. The Na(+)-TtCutA1 structure unveils a dodecameric assembly with metal ions in the trimer-trimer interfaces and the lateral clefts of the trimer. For Na(+)-PhCutA1, the metal ion associated with six waters in an octahedral geometry. The structures suggest that CutA1 may contribute to regulating intracellular metal homeostasis through various binding modes.